5t07: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5t07' size='340' side='right'caption='[[5t07]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='5t07' size='340' side='right'caption='[[5t07]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5t07]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5t07]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T07 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.717Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MFK:DECANOYL-COA'>MFK</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t07 OCA], [https://pdbe.org/5t07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t07 RCSB], [https://www.ebi.ac.uk/pdbsum/5t07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t07 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/YBGC_ECOLI YBGC_ECOLI] Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. | ||
==See Also== | ==See Also== | ||
| Line 16: | Line 15: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Anderson | [[Category: Anderson WF]] | ||
[[Category: Di Leo R]] | |||
[[Category: Leo | [[Category: Savchenko A]] | ||
[[Category: Savchenko | [[Category: Skarina T]] | ||
[[Category: Skarina | [[Category: Stogios PJ]] | ||
[[Category: Stogios | [[Category: Watanabe N]] | ||
[[Category: Watanabe | |||
Latest revision as of 12:52, 4 October 2023
Crystal structure of a putative acyl-CoA thioesterase EC709/ECK0725 from Escherichia coli in complex with Decanoyl-CoA
| ||||||||||||
